7G83: Transforming protein RhoA

ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z108545814. Determined by X-ray diffraction at 1.31 Å resolution. Released 12 Jul 2023.

Method: X-ray diffraction
Resolution: 1.31 Å
Organism: Homo sapiens
Chains: 2
Atoms: 4,206
Mol. weight: 50.99 kDa
Ligands: YX2
Released: 12 Jul 2023

Explore 7G83 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7G83 contains 29 α-helices and 6 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	1
α-helix	18-27	10
β-strand	42-48	7	1
β-strand	51-59	9	1
α-helix	70-73	4
β-strand	79-85	7	1
α-helix	89-93	5
α-helix	95-99	5
α-helix	100-106	7
β-strand	112-117	6	1
α-helix	119-121	3
α-helix	125-132	8
α-helix	138-140	3
α-helix	141-151	11
β-strand	155-158	4	1
α-helix	167-179	13

Chain B: 19 helices, 0 β-strands

Element	Residues	Length
α-helix	206-211	6
α-helix	217-220	4
α-helix	223-226	4
α-helix	231-255	25
α-helix	256-262	7
α-helix	263-267	5
α-helix	273-279	7
α-helix	283-304	22
α-helix	306	1
α-helix	319-325	7
α-helix	328-343	16
α-helix	345-358	14
α-helix	360-369	10
α-helix	373-375	3
α-helix	380-390	11
α-helix	391-393	3
α-helix	394-403	10
α-helix	409-431	23
α-helix	442-446	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transforming protein RhoA	A	protein	185	Homo sapiens	P61586 (AlphaFold model)
Rho guanine nucleotide exchange factor 2	B	protein	245	Homo sapiens	Q92974 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7G83_1 Transforming protein RhoA (chains A)
SMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWD
TAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKK
DLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAAL
QARRG

Sequence of entity 2 (B), FASTA

>7G83_2 Rho guanine nucleotide exchange factor 2 (chains B)
SMEMDEKDFAADSWSLAVDSSFLQQHKKEVMKQQDVIYELIQTELHHVRTLKIMTRLFRT
GMLEELHLEPGVVQGLFPCVDELSDIHTRFLSQLLERRRQALCPGSTRNFVIHRLGDLLI
SQFSGPSAEQMCKTYSEFCSRHSKALKLYKELYARDKRFQQFIRKVTRPAVLKRHGVQEC
ILLVTQRITKYPLLISRILQHSHGIEEERQDLTTALGLVKELLSNVDEGIYQLEKGARLQ
EIYNR

Ligands and cofactors

ID	Name	Formula	Copies
YX2	3-propanamido-1-benzofuran-2-carboxamide	C12 H12 N2 O3	2

Water and common crystallization additives (FMT, DMS) are not listed.

Primary citation

ARHGEF2 PanDDA analysis group deposition. Bradshaw, W.J., Katis, V.L., Bountra, C. et al. To be published.

Other PDB entries of the same protein (UniProt P61586 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6V6U 1.16 Å, Crystal structure of RhoA-GDP with novel Switch I conformation
5C4M 1.3 Å, RhoA GDP with novel switch II conformation
7G8T 1.39 Å, ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z1273312142
6V6M 1.39 Å, Crystal structure of an inactive state of GMPPNP-bound RhoA
6V6V 1.4 Å, Crystal structure of oncogenic RhoA mutant G14V complexed with GDP
8BNT 1.4 Å, The DH domain of ARHGEF2 bound to RhoA
8FPW 1.4 Å, Crystal structure of tumor related RhoA mutant A161V in complex with GDP
8GI6 1.4 Å, Crystal structure of RhoA mutant L69R complexed with GDP
6BCB 1.4 Å, A Complex between PH Domain of p114RhoGEF and Activated RhoA Bound to a GTP Analog
7G82 1.41 Å, ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z1079512010
5C2K 1.42 Å, Crystal structure of the fusion protein linked by RhoA and the GAP domain of MgcRacGAP
7G8B 1.42 Å, ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z100643660

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